Efficient accommodation of recombinant, foot-and-mouth disease virus RGD peptides to cell-surface integrins

The engineering of either complete virus cell-binding proteins or derived l igand peptides generates promising nonviral vectors for cell targeting and gene therapy. In this work, we have explored the molecular interaction betw een a recombinant, integrin-binding foot-and-mouth disease virus RGD peptid e displayed on the surface of a carrier protein and its receptors on the ce ll surface. By increasing the number of viral segments, cell binding to rec ombinant proteins was significantly improved. This fact resulted in a drama tic growth stimulation of virus-sensitive BHK21 cells but not virus-resista nt HeLa cells in protein-coated wells. Surprisingly, growth stimulation was not observed in vitronectin-coated plates, suggesting that integrins other than alpha (v)beta (3) could be involved in binding of the recombinant pep tide, maybe as coreceptors. On the other hand, both free and cell-linked in tegrins did not modify the enzymatic activity of BOB-based enzymatic sensor s that contrarily, were activated by the induced fit of anti-BOB antibodies . Those findings are discussed in the context of a proper mimicry of the un usually complex architecture of this cell-binding site as engineered in mul tifunctional proteins. (C) 2001 Academic Press.